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Ohshima, Hiroyuki; Morishita, Masaki*; Aizawa, Kosuke; Ando, Masanori; Ashida, Takashi; Chikazawa, Yoshitaka; Doda, Norihiro; Enuma, Yasuhiro; Ezure, Toshiki; Fukano, Yoshitaka; et al.
Sodium-cooled Fast Reactors; JSME Series in Thermal and Nuclear Power Generation, Vol.3, 631 Pages, 2022/07
This book is a collection of the past experience of design, construction, and operation of two reactors, the latest knowledge and technology for SFR designs, and the future prospects of SFR development in Japan. It is intended to provide the perspective and the relevant knowledge to enable readers to become more familiar with SFR technology.
Ishigami, Keisuke*; Yoshimatsu, Kohei*; Toyota, Daisuke*; Takizawa, Masaru*; Yoshida, Teppei*; Shibata, Goro*; Harano, Takayuki*; Takahashi, Yukio*; Kadono, Toshiharu*; Verma, V. K.*; et al.
Physical Review B, 92(6), p.064402_1 - 064402_5, 2015/08
Times Cited Count:42 Percentile:83.69(Materials Science, Multidisciplinary)Murakami, Hiroshi; Toyota, Yuji*; Nishi, Takaki*; Nashima, Shigeki*
Chemical Physics Letters, 519-520, p.105 - 109, 2012/01
Times Cited Count:18 Percentile:55.75(Chemistry, Physical)no abstracts in English
Murakami, Hiroshi; Nishi, Takaki*; Toyota, Yuji*
Journal of Physical Chemistry B, 115(19), p.5877 - 5885, 2011/04
Times Cited Count:15 Percentile:35.3(Chemistry, Physical)We present a method based on near-infrared absorption spectroscopy of the OH stretching vibration band of water around 3400 cm to examine if the aqueous cavity size of a protein-unfilled reverse micelle is affected by solubilization of protein, and it has been found for AOT (= bis (2-ethylhexyl) sulfosuccinate) reverse micellar solution with myoglobin that it does not change before and after solubilization of the protein in the water-to-surfactant molar ratio () from 2 to 18, that is, the values of the protein-filled and unfilled reverse micelles are the same as that of the reverse micellar solution regardless of size relation between the aqueous cavity of the unfilled reverse micelle and the protein. On the basis of this experimental fact, we propose a model to determine the structural parameters of protein-filled reverse micelles, such as the aqueous cavity radius and the aggregation number of surfactant molecules constituting the micelle, and the molar concentration of the unfilled reverse micelle that exists with the protein-filled reverse micelle in the reverse micellar solution, and derive their values for AOT reverse micellar solution with myoglobin in the range from 2 to 24. On the other hand, circular dichroism measurements and UV-visible absorption spectroscopy of myoglobin/AOT reverse micellar solution and myoglobin/AOT aqueous solution were carried out in order to examine the conformational state of myoglobin in the reverse micellar solution. These experimental results lead to the conclusion that myoglobin is located in the aqueous cavity of the reverse micelle, although the conformational state of the protein is to some extent distorted because of the interaction with AOT compared with that of native myoglobin. Finally, it is suggested that the proposed model is appropriate for reverse micellar solution with a hydrophilic protein molecule that is located in the aqueous cavity of the reverse micelle.
Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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no abstracts in English
Murakami, Hiroshi; Toyota, Yuji; Nishi, Takaki
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Toyota, Yuji; Nishi, Takaki; Murakami, Hiroshi; Nashima, Shigeki*; Hosoda, Makoto*
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki; Toyota, Yuji
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Murakami, Hiroshi; Nishi, Takaki*; Toyota, Yuji*; Ono, Masato
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Murakami, Hiroshi; Nishi, Takaki*; Toyota, Yuji*
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no abstracts in English